Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Tracking Transitions in Spider Wrapping Silk Conformation and Dynamics by (19)F Nuclear Magnetic Resonance Spectroscopy.

Biochemistry - 31 May 2016

Sarker Muzaddid, Orrell Kathleen E, Xu Lingling, Tremblay Marie-Laurence, Bak Jessi J, Liu Xiang-Qin, Rainey Jan K

Abstract excerpt

Aciniform silk protein (AcSp1) is the primary component of wrapping silk, the toughest of the spider silks because of a combination of high tensile strength and extensibility. Argiope trifasciata AcSp1 contains a core repetitive domain with at least 14 homogeneous 200-amino acid units ("W" units). Upon fibrillogenesis, AcSp1 converts from an α-helix-rich soluble state to a mixed α-helical/β-sheet conformation....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Circular Dichroism
Share to Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Spiders

Share to Tensile Strength

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 27153372
DOI: 10.1021/acs.biochem.6b00429
PMCID: PMC5770200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tracking Transitions in Spider Wrapping Silk Conformation and Dynamics by (19)F Nuclear Magnetic Resonance Spectroscopy.PMID 27153372Read ↗

Engineered disulfides improve mechanical properties of recombinant spider silk.Semantic proximity Read ↗

Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.Semantic proximity Read ↗

Structure and function of C-terminal domain of aciniform spidroin.Semantic proximity Read ↗

19F NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2.Semantic proximity Read ↗

(19)F nuclear magnetic resonance and crystallographic studies of 5-fluorotryptophan-labeled anthrax protective antigen and effects of the receptor on stability.Semantic proximity Read ↗

Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and fiber formation.Semantic proximity Read ↗

Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using 19F NMR.Semantic proximity Read ↗

Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR.Semantic proximity Read ↗

Solution 19F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin.Semantic proximity Read ↗

Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Semantic proximity Read ↗

Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies.Semantic proximity Read ↗

Design of silk proteins with increased heme binding capacity and fabrication of silk-heme materials.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.